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Breakthroughs in the discovery and use of different peroxidase isoforms of microbial origin

  • Received: 29 July 2020 Accepted: 20 September 2020 Published: 22 September 2020
  • Peroxidases are classified as oxidoreductases and are the second largest class of enzymes applied in biotechnological processes. These enzymes are used to catalyze various oxidative reactions using hydrogen peroxide and other substrates as electron donors. They are isolated from various sources such as plants, animals and microbes. Peroxidase enzymes have versatile applications in bioenergy, bioremediation, dye decolorization, humic acid degradation, paper and pulp, and textile industries. Besides, peroxidases from different sources have unique abilities to degrade a broad range of environmental pollutants such as petroleum hydrocarbons, dioxins, industrial dye effluents, herbicides and pesticides. Ironically, unlike most biological catalysts, the function of peroxidases varies according to their source. For instance, manganese peroxidase (MnP) of fungal origin is widely used for depolymerization and demethylation of lignin and bleaching of pulp. While, horseradish peroxidase of plant origin is used for removal of phenols and aromatic amines from waste waters. Microbial enzymes are believed to be more stable than enzymes of plant or animal origin. Thus, making microbially-derived peroxidases a well-sought-after biocatalysts for versatile industrial and environmental applications. Therefore, the current review article highlights on the recent breakthroughs in the discovery and use of peroxidase isoforms of microbial origin at a possible depth.

    Citation: Pontsho Patricia Twala, Alfred Mitema, Cindy Baburam, Naser Aliye Feto. Breakthroughs in the discovery and use of different peroxidase isoforms of microbial origin[J]. AIMS Microbiology, 2020, 6(3): 330-349. doi: 10.3934/microbiol.2020020

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  • Peroxidases are classified as oxidoreductases and are the second largest class of enzymes applied in biotechnological processes. These enzymes are used to catalyze various oxidative reactions using hydrogen peroxide and other substrates as electron donors. They are isolated from various sources such as plants, animals and microbes. Peroxidase enzymes have versatile applications in bioenergy, bioremediation, dye decolorization, humic acid degradation, paper and pulp, and textile industries. Besides, peroxidases from different sources have unique abilities to degrade a broad range of environmental pollutants such as petroleum hydrocarbons, dioxins, industrial dye effluents, herbicides and pesticides. Ironically, unlike most biological catalysts, the function of peroxidases varies according to their source. For instance, manganese peroxidase (MnP) of fungal origin is widely used for depolymerization and demethylation of lignin and bleaching of pulp. While, horseradish peroxidase of plant origin is used for removal of phenols and aromatic amines from waste waters. Microbial enzymes are believed to be more stable than enzymes of plant or animal origin. Thus, making microbially-derived peroxidases a well-sought-after biocatalysts for versatile industrial and environmental applications. Therefore, the current review article highlights on the recent breakthroughs in the discovery and use of peroxidase isoforms of microbial origin at a possible depth.


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    Acknowledgment



    The authors express their deepest gratitude to the research team at OMICS Research Group and Research Facility at the Department of Biotechnology, Vaal University of Technology for their technical support. The funding was provided by South African Bio-Design Initiative (SABDI) grant number 420/01 SABDI 16/1021 secured by Dr NA Feto.

    Conflict of interest



    The authors declare that they have no conflict of interest.

    Ethical approval



    This article does not contain any studies with human participants or animals performed by any of the authors.

    Funding



    The project was supported by South African Bio-Design Initiative (SABDI) grant number 420/01 SABDI 16/1021 secured by Dr NA Feto.

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